ID AT2A2_FELCA Reviewed; 997 AA.
AC Q00779;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
DE Short=SERCA2;
DE Short=SR Ca(2+)-ATPase 2;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump 2;
DE AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform;
DE AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
GN Name=ATP2A2;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=1535224; DOI=10.1016/0167-4781(92)90078-e;
RA Gambel A.M., Gallien T.N., Dantzler-Whitworth T., Bowes J., Menick D.R.;
RT "Sequence of the feline cardiac sarcoplasmic reticulum Ca(2+)-ATPase.";
RL Biochim. Biophys. Acta 1131:203-206(1992).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol to the
CC sarcoplasmic reticulum lumen. Involved in autophagy in response to
CC starvation. Upon interaction with VMP1 and activation, controls ER-
CC isolation membrane contacts for autophagosome formation. Also modulates
CC ER contacts with lipid droplets, mitochondria and endosomes (By
CC similarity). In coordination with FLVCR2 mediates heme-stimulated
CC switching from mitochondrial ATP synthesis to thermogenesis (By
CC similarity). {ECO:0000250|UniProtKB:O55143,
CC ECO:0000250|UniProtKB:P16615}.
CC -!- FUNCTION: [Isoform 1]: Involved in the regulation of the
CC contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated
CC Ca(2+) signaling pathways via its interaction with TMEM64 which is
CC critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS
CC generation necessary for proper osteoclast generation. Association
CC between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking
CC for activation of NFATC1 and production of mitochondrial ROS, thereby
CC triggering Ca(2+) signaling cascades that promote osteoclast
CC differentiation and activation. {ECO:0000250|UniProtKB:O55143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000250|UniProtKB:P16615};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000250|UniProtKB:P16615};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11607};
CC -!- ACTIVITY REGULATION: Has different conformational states with
CC differential Ca2+ affinity. The E1 conformational state (active form)
CC shows high Ca(2+) affinity, while the E2 state exhibits low Ca(2+)
CC affinity. Reversibly inhibited by phospholamban (PLN) at low calcium
CC concentrations. Inhibited by sarcolipin (SLN) and myoregulin (MRLN).
CC The inhibition is blocked by VMP1 (By similarity). Enhanced by DWORF;
CC DWORF increases activity by displacing sarcolipin (SLN), phospholamban
CC (PLN) and myoregulin (MRLN) (By similarity). Stabilizes SERCA2 in its
CC E2 state (By similarity). {ECO:0000250|UniProtKB:O55143,
CC ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBUNIT: Interacts with sarcolipin (SLN); the interaction inhibits
CC ATP2A2 Ca(2+) affinity. Interacts with phospholamban (PLN); the
CC interaction inhibits ATP2A2 Ca(2+) affinity (By similarity). Interacts
CC with myoregulin (MRLN) (By similarity). Interacts with DWORF (By
CC similarity). Interacts with HAX1 (By similarity). Interacts with S100A8
CC and S100A9 (By similarity). Interacts with SLC35G1 and STIM1. Interacts
CC with TMEM203 (By similarity). Interacts with TMEM64 and PDIA3 (By
CC similarity). Interacts with TMX1 (By similarity). Interacts with TMX2
CC (By similarity). Interacts with VMP1; VMP1 competes with PLN and SLN to
CC prevent them from forming an inhibitory complex with ATP2A2. Interacts
CC with ULK1 (By similarity). Interacts with S100A1 in a Ca(2+)-dependent
CC manner (By similarity). Interacts with TUNAR (By similarity). Interacts
CC with FLVCR2; this interaction occurs in the absence of heme and
CC promotes ATP2A2 proteasomal degradation; this complex is dissociated
CC upon heme binding. Interacts with FNIP1. {ECO:0000250|UniProtKB:O55143,
CC ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with TRAM2 (via C-terminus).
CC {ECO:0000250|UniProtKB:P16615}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein
CC {ECO:0000255}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER
CC contact junction. {ECO:0000250|UniProtKB:O55143}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ATP2A2A, SERCA2a;
CC IsoId=Q00779-1; Sequence=Displayed;
CC Name=2; Synonyms=ATP2A2B, SERCA2b;
CC IsoId=Q00779-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the heart.
CC -!- DOMAIN: Ca(2+) and ATP binding cause major rearrangements of the
CC cytoplasmic and transmembrane domains. According to the E1-E2 model,
CC Ca(2+) binding to the cytosolic domain of the pump in the high-affinity
CC E1 conformation is followed by the ATP-dependent phosphorylation of the
CC active site Asp, giving rise to E1P. A conformational change of the
CC phosphoenzyme gives rise to the low-affinity E2P state that exposes the
CC Ca(2+) ions to the lumenal side and promotes Ca(2+) release.
CC Dephosphorylation of the active site Asp mediates the subsequent return
CC to the E1 conformation. {ECO:0000250|UniProtKB:P04191}.
CC -!- DOMAIN: PLN and SLN both have a single transmembrane helix; both occupy
CC a similar binding site that is situated between the ATP2A2
CC transmembrane helices. {ECO:0000250|UniProtKB:P04191}.
CC -!- PTM: Nitrated under oxidative stress. Nitration on the two tyrosine
CC residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia,
CC leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; Z11500; CAA77576.1; -; mRNA.
DR PIR; S23444; S23444.
DR RefSeq; NP_001009216.1; NM_001009216.1. [Q00779-1]
DR AlphaFoldDB; Q00779; -.
DR SMR; Q00779; -.
DR STRING; 9685.ENSFCAP00000024370; -.
DR PaxDb; 9685-ENSFCAP00000024370; -.
DR GeneID; 493691; -.
DR KEGG; fca:493691; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; Q00779; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0086039; F:P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
DR GO; GO:0140056; P:organelle localization by membrane tethering; ISS:UniProtKB.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IBA:GO_Central.
DR CDD; cd02083; P-type_ATPase_SERCA; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF18; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 2; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Disulfide bond; Endoplasmic reticulum; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..997
FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 2"
FT /id="PRO_0000046195"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 274..295
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 314..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 757..776
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 777..786
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 787..807
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 808..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 828..850
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 851..896
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 897..916
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 917..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 930..948
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 949..963
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 964..984
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 985..997
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 575..594
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000250"
FT REGION 787..807
FT /note="Interaction with PLN"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT REGION 788..997
FT /note="Interaction with TMEM64 and PDIA3"
FT /evidence="ECO:0000250|UniProtKB:O55143"
FT REGION 931..942
FT /note="Interaction with PLN"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 767
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11607"
FT BINDING 907
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55143"
FT MOD_RES 294
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT MOD_RES 295
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55143"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11507"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT DISULFID 875..887
FT /evidence="ECO:0000250|UniProtKB:P11607"
SQ SEQUENCE 997 AA; 109712 MW; CEE18D1A1ADA738F CRC64;
MENAHTKTVE EVLGYFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCRMFILD KVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVKCHQYDGL VELATICALC
NDSALDYNEA KGVYKKFGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV
KQKVMSVIRE WGSGSDTLRC LALATHDNPL RREEMNLEDS ANFIKYETNL TFVGCVGMLD
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL
SPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKSEIGIAMG
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKDDNP DFEGVDCAIF ESPYPMTMAL
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP
LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPAILE
//
